title: Molecular evolution of the aldo-keto reductase gene superfamily.
abstract: The aldo-keto reductase enzymes comprise a functionally diverse gene family which catalyze the NADPH-dependant reduction of a variety of carbonyl compounds. The protein sequences of 45 members of this family were aligned and phylogenetic trees were deduced from this alignment using the neighbor-joining and Fitch algorithms. The branching order of these trees indicates that the vertebrate enzymes cluster in three groups, which have a monophyletic origin distinct from the bacterial, plant, and invertebrate enzymes. A high level of conservation was observed between the vertebrate hydroxysteroid dehydrogenase enzymes, prostaglandin F synthase, and rho-crystallin of Xenopus laevis. We infer from the phylogenetic analysis that prostaglandin F synthase may represent a recent recruit to the eicosanoid biosynthetic pathway from the hydroxysteroid dehydrogenase pathway and furthermore that, in the context of gene recruitment, Xenopus laevis rho-crystallin may represent a shared gene.
authors.affiliation: Center for Experimental Therapeutics, 905 Stellar Chance Laboratories, University of Pennsylvania, 422 Curie Boulevard, Philadelphia, PA 19103, USA.
authors.forename: L T
authors.initials: LT
authors.lastname: Seery
authors.forename: P V
authors.initials: PV
authors.lastname: Nestor
authors.forename: G A
authors.initials: GA
authors.lastname: FitzGerald
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D019143:Evolution, Molecular; D010802:Phylogeny; D016415:Sequence Alignment
chemical_list: D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase